1ltq

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{{Seed}}
 
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[[Image:1ltq.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE==
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The line below this paragraph, containing "STRUCTURE_1ltq", creates the "Structure Box" on the page.
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<StructureSection load='1ltq' size='340' side='right'caption='[[1ltq]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ltq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1ltq| PDB=1ltq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ltq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltq OCA], [https://pdbe.org/1ltq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ltq RCSB], [https://www.ebi.ac.uk/pdbsum/1ltq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ltq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KIPN_BPT4 KIPN_BPT4] Acts as a 5'-hydroxyl kinase, a 3'-phosphatase and a 2',3'-cyclic phosphodiesterase. Catalyzes the transfer of the terminal phosphate of ATP to the 5'-hydroxyl termini of ribo- and deoxyribonucleotides. In the presence of ADP the enzyme also catalyzes an exchange reaction. In the exchange reaction, an excess ADP causes the enzyme to transfer the 5' terminal phosphate from phosphorylated DNA to ADP. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1ltq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ltq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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T4 phage polynucleotide kinase (PNK) was identified over 35 years ago and has become a staple reagent for molecular biologists. The enzyme displays 5'-hydroxyl kinase, 3'-phosphatase, and 2',3'-cyclic phosphodiesterase activities against a wide range of substrates. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase. DNA repair enzymes that share conserved motifs with PNK have been identified in eukaryotes. PNK contains two functionally distinct structural domains and forms a homotetramer. The C-terminal phosphatase domain is homologous to the L-2-haloacid dehalogenase family and the N-terminal kinase domain is homologous to adenylate kinase. The active sites have been characterized through structural homology analyses and visualization of bound substrate.
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===CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE===
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Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase.,Galburt EA, Pelletier J, Wilson G, Stoddard BL Structure. 2002 Sep;10(9):1249-60. PMID:12220496<ref>PMID:12220496</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12220496}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ltq" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12220496 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12220496}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus T4]]
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1LTQ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTQ OCA].
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[[Category: Large Structures]]
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[[Category: Galburt EA]]
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==Reference==
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[[Category: Pelletier J]]
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<ref group="xtra">PMID:12220496</ref><references group="xtra"/>
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[[Category: Stoddard BL]]
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[[Category: Enterobacteria phage t4]]
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[[Category: Wilson G]]
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[[Category: Polynucleotide 5'-hydroxy-kinase]]
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[[Category: Galburt, E A.]]
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[[Category: Pelletier, J.]]
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[[Category: Stoddard, B L.]]
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[[Category: Wilson, G.]]
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[[Category: Alpha/beta]]
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[[Category: Kinase]]
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[[Category: P-loop]]
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[[Category: Phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:02:52 2009''
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Current revision

CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE

PDB ID 1ltq

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